• Microbiology and Biotechnology Letters
• /
• v.27 no.3
• /
• pp.203-207
• /
• 1999

V. alginolyticus 138-2, a marine halophilic bacterium, produced an extracellular amylase with a molecular weight of ca. 56,000. The analysis of the digestion products of soluble starch by thin layer chromatography(TLC) revealed that the extracellular amylase of V. alginolyticus 138-2 is a saccharifying-type alpha-amylase. The alpha-amylase activity of the culture supernatant of soluble starch was optimal at pH 6.0 and 45$^{\circ}C$. Ca2+ slightly increased the alpha-amylase activity, whereas Hg2+, An2+, Cu2+, Ni2+, Fe2+, and Mn2+inhibited the enzymatic activity. Alkylating thiol group agent, iodoacetic acid did not affect the alpha-amylase activity, but reduced thiol reagents such as dithiothreitol, cysteine, and beta-mercaptoethanol stimulated theenzymatic activity. On the other hand, even if V. alginolyticus 138-2 is a marine halophilic bacterium, its alpha-amylase activity was significantly inhibited by NaCl.

• Journal of Sericultural and Entomological Science
• /
• v.24 no.2
• /
• pp.73-80
• /
• 1983

1. The varietal difference in amylase activity of the digestive fluid of the 5th instar larvae reared on the artificial diet was investigated, using the parent commercial silkworm varieties of Japanese strain. The amylase activity was large different among silkworm varieties. The activity was strong in Hansaeng-1, Jam 115 and Jam 117, medium in Hansaeng-3, Jam 113, Jam 119, and Jam 201, weak in Jam 107, Jam 121 and Gyeongchu. The amylase of the digestive fluid of ten parent commercial silkworm varieties is possible-(ae) type, compared with ＋(＋$\^$ae/) type of Daizo. 2. To investigate the effect of a-amylase pre-treatment of the artificial diet, larvae were fed with the diet treated by a-amylase during 4th-5th instar periods. The blood sugar content and cocoon qualities were slightly higher in the experimental larvae than those in the control, while showing the slight less body weight, amylase activity and dietary efficient.

• Journal of Plant Biology
• /
• v.11 no.1
• /
• pp.1-6
• /
• 1968

The effects of the different temperatures on the amylase activity and growth rate of the rye seedling grown in the solutions containing radioactive sulfur- 35 were studied. The amylase activity of the coleoptiles obtained from the seedlings grown in the solutions of S-35, at 14$^{\circ}C$, appeared to be strongly stimulated in comparison to the control, but the culture temperatures of 22$^{\circ}C$ and 3$0^{\circ}C$ showed the decrease in the amylase activity. The amylase activity of the grains treated with the low intensity of the ratioactive material didn't show clear changes, at any culture temperatures, but the amylase activity of the grains treated with the high intensity of S-35, 50$\mu$c, showed definite decline at the elevated culture temperature, 3$0^{\circ}C$. Similar effects was also found in the growth of the seedlings. However, we would consider the effects of the radioactive materials on the acticity of the amylase and the growth of the seedlings are resulted from the accumulation of the much amount of the radioactive materials, and this accumulation rate depends upon actually the elevation of the culture temperature.

• Journal of Plant Biology
• /
• v.26 no.4
• /
• pp.173-180
• /
• 1983

L-canavanine was added to GAs treated barley seeds, and induced amylase activity, soluble protein content, and arginine content were mesured. Canavanine, added at the beginning of the incubation period, inhibited amylase activity and protein accumulation. Amylase activity decreased markedly by addition of canavanine at 6 hr after incubation, where soluble protein content was not affected. The addition of canavanine after 12 hr incubation did not show serioud inhibited effect on the amylase activity and protein accumulation. GAs incubation caused decrement in arginine content per mg protein, but it was somewhat recovered by canavanine treatment. The longer the time between GAs and canavanine addition was, the less the recovery ration was. Arginine content in the $\alpha$-amylase fraction (ammonium sulfate 20~50% saturation) was lower than in 0~20% fraction, but higher than in 50~80% fraction. These results and control expreiments, using cordycepin and cycloheximide, support the idea that canavanine might incorporate into protein.

• Korean journal of food and cookery science
• /
• v.14 no.3
• /
• pp.261-265
• /
• 1998

The activity and characteristics of ${\alpha}$-amylase in soy milk as well as in Jeungpyun batters were determined to investigate the enzyme system related to Jeungpyun preparation. ${\alpha}$-Amylase activity was detected in soy milk as well as in Jeungpyun batters. Soy milk had ${\alpha}$-amylase activity of 0.79 units/mg protein for gelatinized starch and 0.036 units/mg protein for raw starch. ${\alpha}$-Amylase in soy milk showed maximum activities at pH 5.92∼6.87 and at 60$^{\circ}C$ for both gelatinized starch and raw starch. ${\alpha}$-Amylase activities of Jeungpyun batters containing soy milk were 25.59 units/mg protein for gelatinized starch and 1.37 units/mg protein for raw starch. Jeungpyun batters without soy milk demonstrated ${\alpha}$-amylase activities of 3.37 units/mg protein for gelatinized starch and 0.49 units/mg protein for raw starch. ${\alpha}$-Amylase of Jeungpyun batters showed an optimal activity at pH 5.25 and at 60$^{\circ}C$ for both gelatinized and raw starch. The results demonstrated that Jeungpyun batters with soy milk showed significantly higher ${\alpha}$-amylase activity than the ones without soy milk.

• YAKHAK HOEJI
• /
• v.4 no.1
• /
• pp.35-38
• /
• 1959

The enzymatic activity of amylase which was isolated from a shell fish Veneridae Soxidmnus purpuratus Sowerby(Korean name :Gai-jo-gai") was studied and the obtained results were as follows: (1) The optimum pH of the enzyme was Ca. 6.2-6.4. (2) Prohibiting activity of metalic ions for the enzymatic activity was the order of 1/1000M-$Mg^{++}$>1/1000M-$Sr^{++}$>1/1000M-$Na^{+}$, and $Ca^{++}$ ion's prohibiting action was hardly showed. (3) Of 3 specimens of amyiase from Heptapancreas, Gastro-intestine and crystalline style, the highest activity was shown by amylase from crystlline style, and the other two showed almost same degree of activity. (4) Heptapancreas Amylase from the shell fish showed remarkably higher enzymatic activity than the pancreas amylase from a pig.

• The Korean Journal of Food And Nutrition
• /
• v.33 no.2
• /
• pp.210-214
• /
• 2020

In this study, polyphenol and flavonoid contents were measured, and DPPH, OH, H₂O₂ radical scavenging activity, and the α-amylase inhibitory activity were measured to study the antioxidant activity of 70% ethanol extract from Morinda citrifolia L. The polyphenol and flavonoid contents of noni 70% ethanol extract were 29.52 GAE/g and 12.48 CE/g, respectively. Also, the IC₅₀ values of DPPH, hydroxyl radical, and hydrogen peroxide scavenging activity of 70% ethanol extract from noni were 18.70 mg/mL, 26.45 mg/mL, and 35.67 mg/mL, respectively. Measurement of the α-amylase inhibitory activity of 70% ethanol extract from noni showed 45% inhibitory activity at 10 mg/mL.

• Asian-Australasian Journal of Animal Sciences
• /
• v.19 no.8
• /
• pp.1164-1173
• /
• 2006

Cellulase from Aspergillus niger, (${\alpha}$-amylase from Bacillus sp. and protease from Bacillus globigii were used as enzyme sources in this study to examine how their respective substrates protect them in two kinds of simulated gastrointestinal tract digesting processes. Avian total digest tract simulation test showed that filter paper, Avicel and cellulose resulted in 7.7, 6.4 and 7.4 times more activity than of unprotected cellulose, respectively. Protease with addition of casein, gelatin or soybean protein showed no significant protection response. Starch protected amylase to be 2.5 times activity of the unprotected one. Monogastric animal total tract digestion simulation test showed that filter paper, Avicel and cellulose resulted in 5.9, 9.0 and 8.8 times activity of unprotected cellulase, respectively. Casein, gelatin and soybean protein resulted in 1.2, 1.3 and 2.0 times activity of unprotected protease, respectively. Starch did not protect amylase activity in monogastric animal total tract simulation. Protection of mixed enzymes by substrates in two animal total tract simulation tests showed that filter paper in combination with soybean protein resulted in 1.5 times activity of unprotected cellulose, but all substrates tested showed no significant protection effect to protease. Soybean protein and starch added at the same time protected the amylase activity to be two times of the unprotected one. Test of non-purified substrate protection in two animal total digest tract simulation showed that cellulase activity increased as BSA (bovine serum albumin) concentration increased, with the highest activity to be 1.3 times of unprotected enzyme. However, BSA showed no significant protection effect to protease. Amylase activity increased to 1.5 times as BSA added more than 1.5% (w/v). Cellulase activity increased to 1.5 times as soybean hull was added higher than 1.5%. Amylase had a significant protection response only when soybean hull added up to 2%. Protease activity was not protected by soybean hull to any significant extent.

• YAKHAK HOEJI
• /
• v.5 no.1
• /
• pp.45-50
• /
• 1960

Some enzymatic properties of Cynthia roretzi v. (Drasche Korean : U-Rung-Shei) was studied by author and obtained the following results; 1. The optimum pH of the digestive gland amylase was 6.8-7.0 2. Activity of metallic ion on the amylase showed the following order; 10$^{-3}$ M M $n^{++}$>10$^{-3}$ M $Co^{++}$>10$^{-4}$ M $Mg^{++}$>10$^{-4}$ M $Ca^{++}$>10$^{-2}$ M Z $n^{++}$>10$^{-2}$ M P $b^{++}$ 3. The digestive gland enzyme inactivated at 70.deg. C. 4. When the enzyme concentration increase 2 times, the enzymatic activity also increase, but not propertionally. 5. The digestine gland amylase showed remarkably higher enzymatic activity than the intestinal amylase. 6. The digestive gland amylase from the ascidian showed remarkably higher enzymatic activity than the heptancreatic amylase from shell fish (Turbo (Batillus) Cornutus Solander).nder).nder).

• Korean Journal of Food Science and Technology
• /
• v.31 no.6
• /
• pp.1421-1426
• /
• 1999

Sixteen domestic barley varieties and subsequently produced malts were evaluated for quality characteristics. Diastatic power(DP), complementary actions of amylases in malt, had a wide $variation(139{\sim}220^{\circ}L)$ among the barley varieties. Some 6-row barley varieties demonstrated significantly high DP values. ${\beta}-\;and\;{\alpha}-amylase$ activities in malts were also significantly influenced by barley varieties. Diastatic power was highly correlated with ${\beta}-amylase$ activity, indicating that the ${\beta}-amylase$ activity was a predominant factor determining saccharifying action in malt. Amylograph was used to indirectly estimate starch-degrading enzymatic activity, and the reduction in amylograph viscosity was associated with ${\alpha}-amylase$ activity. Barley quality factors in relation to enzymatic activity of malt were analyzed, and the barley variety with lower kernel weight and less plumper kernels tended to produce higher starch-degrading enzyme activity. Potential diastatic power, an estimate of bound ${\beta}-amylase$ in raw barley, was associated with diastatic power in the final malt. Potential diastatic power turned out to be an important factor for predicting good malting barley.